Prof Michael Hough

Rose, SL., Ferroni, FM., Horrell, S., Brondino, CD., Eady, RR., Jaho, S., Hough, MA., Owen, RL., Antonyuk, SV. and Hasnain, SS., (2024). Spectroscopically Validated pH-dependent MSOX Movies Provide Detailed Mechanism of Copper Nitrite Reductases. Journal of Molecular Biology. 436 (18), 168706-168706

Fujii, S., Wilson, MT., Adams, HR., Mikolajek, H., Svistunenko, DA., Smyth, P., Andrew, CR., Sambongi, Y. and Hough, MA., (2024). Conformational rigidity of cytochrome c'-α from a thermophile is associated with slow NO binding. Biophysical Journal. 123 (16), 2594-2603

Jaho, S., Axford, D., Gu, D-H., Hough, MA. and Owen, RL., (2024). Use of fixed targets for serial crystallography. Methods in Enzymology. 709, 29-55

Hough, MA., Prischi, F. and Worrall, JAR., (2023). Perspective: Structure determination of protein-ligand complexes at room temperature using X-ray diffraction approaches. Frontiers in Molecular Biosciences. 10, 1113762-

Adams, HR., Svistunenko, DA., Wilson, MT., Fujii, S., Strange, RW., Hardy, ZA., Vazquez, PA., Dabritz, T., Streblow, GJ., Andrew, CR. and Hough, MA., (2023). A heme pocket aromatic quadrupole modulates gas binding to cytochrome c'-β: Implications for NO sensors.. Journal of Biological Chemistry. 299 (6), 104742-104742

Mikolajek, H., Sanchez-Weatherby, J., Sandy, J., Gildea, RJ., Campeotto, I., Cheruvara, H., Clarke, JD., Foster, T., Fujii, S., Paulsen, IT., Shah, BS. and Hough, MA., (2023). Protein-to-structure pipeline for ambient-temperature in situ crystallography at VMXi. IUCrJ. 10 (4), 420-429

Agirre, J., Atanasova, M., Bagdonas, H., Ballard, CB., Baslé, A., Beilsten-Edmands, J., Borges, RJ., Brown, DG., Burgos-Mármol, JJ., Berrisford, JM., Bond, PS., Caballero, I., Catapano, L., Chojnowski, G., Cook, AG., Cowtan, KD., Croll, TI., Debreczeni, JÉ., Devenish, NE., Dodson, EJ., Drevon, TR., Emsley, P., Evans, G., Evans, PR., Fando, M., Foadi, J., Fuentes-Montero, L., Garman, EF., Gerstel, M., Gildea, RJ., Hatti, K., Hekkelman, ML., Heuser, P., Hoh, SW., Hough, MA., Jenkins, HT., Jiménez, E., Joosten, RP., Keegan, RM., Keep, N., Krissinel, EB., Kolenko, P., Kovalevskiy, O., Lamzin, VS., Lawson, DM., Lebedev, AA., Leslie, AGW., Lohkamp, B., Long, F., Malý, M., McCoy, AJ., McNicholas, SJ., Medina, A., Millán, C., Murray, JW., Murshudov, GN., Nicholls, RA., Noble, MEM., Oeffner, R., Pannu, NS., Parkhurst, JM., Pearce, N., Pereira, J., Perrakis, A., Powell, HR., Read, RJ., Rigden, DJ., Rochira, W., Sammito, M., Sánchez Rodríguez, F., Sheldrick, GM., Shelley, KL., Simkovic, F., Simpkin, AJ., Skubak, P., Sobolev, E., Steiner, RA., Stevenson, K., Tews, I., Thomas, JMH., Thorn, A., Valls, JT., Uski, V., Usón, I., Vagin, A., Velankar, S., Vollmar, M., Walden, H., Waterman, D., Wilson, KS., Winn, MD., Winter, G., Wojdyr, M. and Yamashita, K., (2023). The CCP4 suite: integrative software for macromolecular crystallography. Acta Crystallographica Section D Structural Biology. 79 (6), 449-461

Lučić, M., Wilson, MT., Pullin, J., Hough, MA., Svistunenko, DA. and Worrall, JAR., (2023). New insights into controlling radical migration pathways in heme enzymes gained from the study of a dye-decolorising peroxidase. Chemical Science. 14 (44), 12518-12534

Yoshimi, T., Fujii, S., Oki, H., Igawa, T., Adams, HR., Ueda, K., Kawahara, K., Ohkubo, T., Hough, MA. and Sambongi, Y., (2022). Crystal structure of thermally stable homodimeric cytochrome c′-β from Thermus thermophilus. Acta Crystallographica Section F Structural Biology Communications. 78 (6), 217-225

Moreno-Chicano, T., Carey, LM., Axford, D., Beale, JH., Doak, RB., Duyvesteyn, HME., Ebrahim, A., Henning, RW., Monteiro, DCF., Myles, DA., Owada, S., Sherrell, DA., Straw, ML., Šrajer, V., Sugimoto, H., Tono, K., Tosha, T., Tews, I., Trebbin, M., Strange, RW., Weiss, KL., Worrall, JAR., Meilleur, F., Owen, RL., Ghiladi, RA. and Hough, MA., (2022). Complementarity of neutron, XFEL and synchrotron crystallography for defining the structures of metalloenzymes at room temperature. IUCrJ. 9 (5), 610-624

Worrall, JAR. and Hough, MA., (2022). Serial femtosecond crystallography approaches to understanding catalysis in iron enzymes.. Current Opinion in Structural Biology. 77, 102486-102486

Lučić, M., Wilson, MT., Tosha, T., Sugimoto, H., Shilova, A., Axford, D., Owen, RL., Hough, MA. and Worrall, JAR., (2022). Serial Femtosecond Crystallography Reveals the Role of Water in the One- or Two-Electron Redox Chemistry of Compound i in the Catalytic Cycle of the B-Type Dye-Decolorizing Peroxidase DtpB. ACS Catalysis. 12 (21), 13349-13359

Horrell, S., Axford, D., Devenish, NE., Ebrahim, A., Hough, MA., Sherrell, DA., Storm, SLS., Tews, I., Worrall, JAR. and Owen, RL., (2021). Fixed Target Serial Data Collection at Diamond Light Source.. Journal of Visualized Experiments. 2021 (168)

McKew, BA., Johnson, R., Clothier, L., Skeels, K., Ross, MS., Metodiev, M., Frenzel, M., Gieg, LM., Martin, JW., Hough, MA. and Whitby, C., (2021). Differential protein expression during growth on model and commercial mixtures of naphthenic acids in Pseudomonas fluorescens Pf‐5. MicrobiologyOpen. 10 (4), e1196-

Sen, K., Hough, MA., Strange, RW., Yong, C. and Keal, TW., (2021). QM/MM Simulations of Protein Crystal Reactivity Guided by MSOX Crystallography: A Copper Nitrite Reductase Case Study.. The Journal of Physical Chemistry B: Biophysical Chemistry, Biomaterials, Liquids, and Soft Matter. 125 (32), 9102-9114

Lučić, M., Wilson, MT., Svistunenko, DA., Owen, RL., Hough, MA. and Worrall, JAR., (2021). Aspartate or arginine? Validated redox state X-ray structures elucidate mechanistic subtleties of FeIV = O formation in bacterial dye-decolorizing peroxidases. Journal of Biological Inorganic Chemistry. 26 (7), 743-761

Hough, MA. and Owen, RL., (2021). Serial synchrotron and XFEL crystallography for studies of metalloprotein catalysis. Current Opinion in Structural Biology. 71, 232-238

Stohrer, C., Horrell, S., Meier, S., Sans, M., von Stetten, D., Hough, M., Goldman, A., Monteiro, DCF. and Pearson, AR., (2021). Homogeneous batch micro-crystallization of proteins from ammonium sulfate. Acta Crystallographica Section D: Structural Biology. 77 (2), 194-204

Lucic, M., Chaplin, AK., Moreno-Chicano, T., Dworkowski, F., Wilson, M., Svistunenko, D., Hough, M. and Worrall, JAR., (2020). A subtle structural change in the distal haem pocket has a remarkable effect on tuning hydrogen peroxide reactivity in dye decolourising peroxidases from Streptomyces lividans. Dalton Transactions. 49 (5), 1620-1636

Lucic, M., Svistunenko, D., Wilson, M., Chaplin, A., Davy, B., Ebrahim, A., Axford, D., Tosha, T., Sugimoto, H., Owada, S., Dworkowski, F., Tews, I., Owen, R., Hough, M. and Worrall, JAR., (2020). Serial femtosecond zero dose crystallography captures a water‐free distal heme site in a dye‐decolourising peroxidase to reveal a catalytic role for an arginine in FeIV=O formation. Angewandte Chemie International Edition. 59 (48), 21656-21662

Brown, BN., Robinson, KJ., Durfee, QC., Kekilli, D., Hough, MA. and Andrew, CR., (2020). Hydroxylamine Complexes of Cytochrome c': Influence of Heme Iron Redox State on Kinetic and Spectroscopic Properties.. Inorganic Chemistry. 59 (19), 14162-14170

Hough, MA., Conradie, J., Strange, RW., Antonyuk, SV., Eady, RR., Ghosh, A. and Hasnain, SS., (2020). Nature of the copper-nitrosyl intermediates of copper nitrite reductases during catalysis. Chemical Science. 11 (46), 12485-12492

Ebrahim, A., Appleby, MV., Axford, D., Beale, J., Moreno-Chicano, T., Sherrell, DA., Strange, RW., Hough, MA. and Owen, RL., (2019). Resolving polymorphs and radiation-driven effects in microcrystals using fixed-target serial synchrotron crystallography. Acta Crystallographica Section D Structural Biology. 75 (2), 151-159

Adams, HR., Krewson, C., Vardanega, JE., Fujii, S., Moreno-Chicano, T., Sambongi, Y., Svistunenko, D., Paps, J., Andrew, CR. and Hough, MA., (2019). One fold, two functions: cytochrome P460 and cytochrome c′-β from the methanotroph Methylococcus capsulatus (Bath). Chemical Science. 10 (10), 3031-3041

Chaplin, AK., Chicano, TM., Hampshire, BV., Wilson, MT., Hough, MA., Svistunenko, DA. and Worrall, JAR., (2019). An Aromatic Dyad Motif in Dye Decolourising Peroxidases Has Implications for Free Radical Formation and Catalysis. Chemistry – A European Journal. 25 (24), 6141-6153

Straw, ML., Hough, MA., Wilson, MT. and Worrall, JAR., (2019). A histidine residue and a tetranuclear cuprous‐thiolate cluster dominate the copper loading landscape of a copper storage protein from Streptomyces lividans. Chemistry – A European Journal. 25 (45), 10678-10688

Ebrahim, A., Moreno-Chicano, T., Appleby, MV., Chaplin, AK., Beale, JH., Sherrell, DA., Duyvesteyn, HME., Owada, S., Tono, K., Sugimoto, H., Strange, RW., Worrall, JAR., Axford, D., Owen, RL. and Hough, MA., (2019). Dose-resolved serial synchrotron and XFEL structures of radiation-sensitive metalloproteins. IUCrJ. 6 (4), 543-551

Moreno-Chicano, T., Ebrahim, A., Axford, D., Appleby, MV., Beale, JH., Chaplin, AK., Duyvesteyn, HME., Ghiladi, RA., Owada, S., Sherrell, DA., Strange, RW., Sugimoto, H., Tono, K., Worrall, JAR., Owen, RL. and Hough, MA., (2019). High-throughput structures of protein–ligand complexes at room temperature using serial femtosecond crystallography. IUCrJ. 6 (6), 1074-1085

Beale, JH., Bolton, R., Marshall, SA., Beale, EV., Carr, SB., Ebrahim, A., Moreno-Chicano, T., Hough, MA., Worrall, JAR., Tews, I. and Owen, RL., (2019). Successful sample preparation for serial crystallography experiments. Journal of Applied Crystallography. 52 (6), 1385-1396

Adams, HR., Krewson, C., Vardanega, JE., Fujii, S., Moreno-Chicano, T., Sambongi, Y., Svistunenko, D., Paps, J., Andrew, CR. and Hough, MA., (2019). Correction: One fold, two functions: cytochrome P460 and cytochrome c′-β from the methanotroph Methylococcus capsulatus (Bath). Chemical Science. 10 (36), 8490-8490

Straw, ML., Chaplin, AK., Hough, MA., Paps, J., Bavro, VN., Wilson, MT., Vijgenboom, E. and Worrall, JAR., (2018). A cytosolic copper storage protein provides a second level of copper tolerance in Streptomyces lividans.. Metallomics: integrated biometal science. 2018 (10), 180-193

Hough, MA. and Wilson, KS., (2018). From crystal to structure with CCP4. Acta Crystallographica. Section d, Structural Biology. 74 (2), 67-67

Horrell, S., Kekilli, D., Sen, K., Owen, RU., Dworkowski, FSN., Antonyuk, SV., Keal, TW., Yong, CW., Eady, RR., Hasnain, SS., Strange, RW. and Hough, MA., (2018). Enzyme catalysis captured using multiple structures from one crystal at varying temperatures. IUCrJ. 5 (3), 283-292

Sen, K., Hough, M., Strange, R., Yong, C. and Keal, T., (2018). A QM/MM Study of Nitrite Binding Modes in a Three-Domain Heme-Cu Nitrite Reductase. Molecules. 23 (11), 2997-2997

Chaplin, AK., Svistunenko, DA., Hough, MA., Wilson, MT., Vijgenboom, E. and Worrall, JAR., (2017). Active site maturation and activity of the copper-radical oxidase GlxA is governed by a tryptophan residue. The Biochemical Journal. 474 (5), 809-825

Kekilli, D., Petersen, CA., Pixton, DA., Ghafoor, DD., Abdullah, GH., Dworkowski, FSN., Wilson, MT., Heyes, DJ., Hardman, SJO., Murphy, LM., Strange, RW., Scrutton, NS., Andrew, CR. and Hough, MA., (2017). Engineering proximal vs. distal heme–NO coordination via dinitrosyl dynamics: implications for NO sensor design. Chemical Science. 8 (3), 1986-1994

McCombs, NL., Moreno-Chicano, T., Carey, LM., Franzen, S., Hough, MA. and Ghiladi, RA., (2017). Interaction of Azole-Based Environmental Pollutants with the Coelomic Hemoglobin from Amphitrite ornata: A Molecular Basis for Toxicity. Biochemistry. 56 (17), 2294-2303

Kekilli, D., Moreno-Chicano, T., Chaplin, AK., Horrell, S., Dworkowski, FSN., Worrall, JAR., Strange, RW. and Hough, MA., (2017). Photoreduction and validation of haem?ligand intermediate states in protein crystals by in situ single-crystal spectroscopy and diffraction. IUCrJ. 4 (3), 263-270

Hough, MA., (2017). Choosing the optimal spectroscopic toolkit to understand protein function. Bioscience Reports. 37 (3), BSR20160378-

Sen, K., Horrell, S., Kekilli, D., Yong, CW., Keal, TW., Atakisi, H., Moreau, DW., Thorne, RE., Hough, MA. and Strange, RW., (2017). Active-site protein dynamics and solvent accessibility in nativeAchromobacter cycloclastescopper nitrite reductase. IUCrJ. 4 (4), 495-505

Horrell, S., Kekilli, D., Strange, RW. and Hough, MA., (2017). Recent structural insights into the function of copper nitrite reductases.. Metallomics. 9 (11), 1470-1482

Nilsson, ZN., Mandella, BL., Sen, K., Kekilli, D., Hough, MA., Moënne-Loccoz, P., Strange, RW. and Andrew, CR., (2017). Distinguishing Nitro vs Nitrito Coordination in Cytochrome c' Using Vibrational Spectroscopy and Density Functional Theory.. Inorganic Chemistry. 56 (21), 13205-13213

Deacon, OM., Karsisiotis, AI., Moreno-Chicano, T., Hough, MA., Macdonald, C., Blumenschein, TMA., Wilson, MT., Moore, GR. and Worrall, JAR., (2017). Heightened Dynamics of the Oxidized Y48H Variant of Human Cytochrome c Increases Its Peroxidatic Activity.. Biochemistry. 56 (46), 6111-6124

Chaplin, AK., Wilson, MT., Hough, MA., Svistunenko, DA., Hemsworth, GR., Walton, PH., Vijgenboom, E. and Worrall, JAR., (2016). Heterogeneity in the Histidine-brace Copper Coordination Sphere in Auxiliary Activity Family 10 (AA10) Lytic Polysaccharide Monooxygenases. Journal of Biological Chemistry. 291 (24), 12838-12850

Horrell, S., Antonyuk, SV., Eady, RR., Hasnain, SS., Hough, MA. and Strange, RW., (2016). Serial crystallography captures enzyme catalysis in copper nitrite reductase at atomic resolution from one crystal. IUCrJ. 3 (4), 271-281

Brooke, GN., Gamble, SC., Hough, MA., Begum, S., Dart, DA., Odontiadis, M., Powell, SM., Fioretti, FM., Bryan, RA., Waxman, J., Wait, R. and Bevan, CL., (2015). Antiandrogens Act as Selective Androgen Receptor Modulators at the Proteome Level in Prostate Cancer Cells*. Molecular & Cellular Proteomics. 14 (5), 1201-1216

Chaplin, AK., Petrus, MLC., Mangiameli, G., Hough, MA., Svistunenko, DA., Nicholls, P., Claessen, D., Vijgenboom, E. and Worrall, JAR., (2015). GlxA is a new structural member of the radical copper oxidase family and is required for glycan deposition at hyphal tips and morphogenesis of Streptomyces lividans. Biochemical Journal. 469 (3), 433-444

Manole, A., Kekilli, D., Svistunenko, DA., Wilson, MT., Dobbin, PS. and Hough, MA., (2015). Conformational control of the binding of diatomic gases to cytochrome c′. JBIC Journal of Biological Inorganic Chemistry. 20 (4), 675-686

Servid, AE., McKay, AL., Davis, CA., Garton, EM., Manole, A., Dobbin, PS., Hough, MA. and Andrew, CR., (2015). Resonance Raman Spectra of Five-Coordinate Heme-Nitrosyl Cytochromes c′: Effect of the Proximal Heme-NO Environment. Biochemistry. 54 (21), 3320-3327

Hough, MA. and Andrew, CR., (2015). Cytochromes c′. RECENT ADVANCES IN MICROBIAL OXYGEN-BINDING PROTEINS. 67, 1-84

Porto, TV., Hough, MA. and Worrall, JAR., (2015). Structural insights into conformational switching in the copper metalloregulator CsoR fromStreptomyces lividans. Acta Crystallographica Section D Biological Crystallography. 71 (9), 1872-1878

Dworkowski, FSN., Hough, MA., Pompidor, G. and Fuchs, MR., (2015). Challenges and solutions for the analysis ofin situ,in crystallomicro-spectrophotometric data. Acta Crystallographica Section D Biological Crystallography. 71 (1), 27-35

Ghafoor, DD., Kekilli, D., Abdullah, GH., Dworkowski, FSN., Hassan, HG., Wilson, MT., Strange, RW. and Hough, MA., (2015). Hydrogen bonding of the dissociated histidine ligand is not required for formation of a proximal NO adduct in cytochrome c’. JBIC Journal of Biological Inorganic Chemistry. 20 (6), 949-956

Reeder, BJ. and Hough, MA., (2014). The structure of a class 3 nonsymbiotic plant haemoglobin fromArabidopsis thalianareveals a novel N-terminal helical extension. Acta Crystallographica Section D Biological Crystallography. 70 (5), 1411-1418

Hough, MA., Silkstone, G., Worrall, JAR. and Wilson, MT., (2014). NO Binding to the Proapoptotic Cytochrome c–Cardiolipin Complex. NITRIC OXIDE. 96, 193-209

Blundell, KLIM., Hough, MA., Vijgenboom, E. and Worrall, JAR., (2014). Structural and mechanistic insights into an extracytoplasmic copper trafficking pathway in Streptomyces lividans. Biochemical Journal. 459 (3), 525-538

Barrier, E., Braz Fernandes, FM., Bujan, M., Feiters, MC., Froideval, A., Ghijsen, J., Hase, T., Hough, MA., Jergel, M., Jimenez, I., Kajander, T., Kikas, A., Kokkinidis, M., Kover, L., Larsen, HB., Lawson, DM., Lawniczak-Jablonska, K., Mariani, C., Mikulik, P., Monnier, J., Morera, S., McGuinness, C., Müller-Buschbaum, P., Meedom Nielson, M., Pietsch, U., Tromp, M., Simon, M., Stangl, J. and Zanotti, G., (2014). The benefit of the European User Community from transnational access to national radiation facilities. Journal of Synchrotron Radiation. 21 (3), 638-639

Kekilli, D., Dworkowski, FSN., Pompidor, G., Fuchs, MR., Andrew, CR., Antonyuk, S., Strange, RW., Eady, RR., Hasnain, SS. and Hough, MA., (2014). Fingerprinting redox and ligand states in haemprotein crystal structures using resonance Raman spectroscopy. Acta Crystallographica Section D Biological Crystallography. 70 (5), 1289-1296

Rajagopal, BS., Edzuma, AN., Hough, MA., Blundell, KLIM., Kagan, VE., Kapralov, AA., Fraser, LA., Butt, JN., Silkstone, GG., Wilson, MT., Svistunenko, DA. and Worrall, JAR., (2013). The hydrogen-peroxide-induced radical behaviour in human cytochrome c–phospholipid complexes: implications for the enhanced pro-apoptotic activity of the G41S mutant. Biochemical Journal. 456 (3), 441-452

Russell, HJ., Hardman, SJO., Heyes, DJ., Hough, MA., Greetham, GM., Towrie, M., Hay, S. and Scrutton, NS., (2013). Modulation of ligand–heme reactivity by binding pocket residues demonstrated in cytochrome c' over the femtosecond–second temporal range. The FEBS Journal. 280 (23), 6070-6082

Dwarakanath, S., Chaplin, AK., Hough, MA., Rigali, S., Vijgenboom, E. and Worrall, JAR., (2012). Response to Copper Stress in Streptomyces lividans Extends beyond Genes under Direct Control of a Copper-sensitive Operon Repressor Protein (CsoR). Journal of Biological Chemistry. 287 (21), 17833-17847

Strange, RW., Hough, MA., Antonyuk, SV. and Hasnain, SS., (2012). Structural Evidence for a Copper-Bound Carbonate Intermediate in the Peroxidase and Dismutase Activities of Superoxide Dismutase. PLoS ONE. 7 (9), e44811-e44811

Doutch, J., Hough, MA., Hasnain, SS. and Strange, RW., (2012). Challenges of sulfur SAD phasing as a routine method in macromolecular crystallography. Journal of Synchrotron Radiation. 19 (1), 19-29

Antonyuk, SV. and Hough, MA., (2011). Monitoring and validating active site redox states in protein crystals. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1814 (6), 778-784

Leferink, NGH., Han, C., Antonyuk, SV., Heyes, DJ., Rigby, SEJ., Hough, MA., Eady, RR., Scrutton, NS. and Hasnain, SS., (2011). Proton-Coupled Electron Transfer in the Catalytic Cycle of Alcaligenes xylosoxidans Copper-Dependent Nitrite Reductase. Biochemistry. 50 (19), 4121-4131

Hough, MA., Antonyuk, SV., Barbieri, S., Rustage, N., McKay, AL., Servid, AE., Eady, RR., Andrew, CR. and Hasnain, SS., (2011). Distal-to-Proximal NO Conversion in Hemoproteins: The Role of the Proximal Pocket. Journal of Molecular Biology. 405 (2), 395-409

Brenner, S., Heyes, DJ., Hay, S., Hough, MA., Eady, RR., Hasnain, SS. and Scrutton, NS., (2009). Demonstration of Proton-coupled Electron Transfer in the Copper-containing Nitrite Reductases. Journal of Biological Chemistry. 284 (38), 25973-25983

Hough, MA., Eady, RR. and Hasnain, SS., (2008). Identification of the Proton Channel to the Active Site Type 2 Cu Center of Nitrite Reductase: Structural and Enzymatic Properties of the His254Phe and Asn90Ser Mutants^,. Biochemistry. 47 (51), 13547-13553

Ellis, MJ., Buffey, SG., Hough, MA. and Hasnain, SS., (2008). On-line optical and X-ray spectroscopies with crystallography: an integrated approach for determining metalloprotein structures in functionally well defined states. Journal of Synchrotron Radiation. 15 (5), 433-439

Hough, MA., Antonyuk, SV., Strange, RW., Eady, RR. and Hasnain, SS., (2008). Crystallography with Online Optical and X-ray Absorption Spectroscopies Demonstrates an Ordered Mechanism in Copper Nitrite Reductase. Journal of Molecular Biology. 378 (2), 353-361

Paraskevopoulos, K., Hough, MA., Sawers, RG., Eady, RR. and Hasnain, SS., (2007). The structure of the Met144Leu mutant of copper nitrite reductase from Alcaligenes xylosoxidans provides the first glimpse of a protein–protein complex with azurin II. JBIC Journal of Biological Inorganic Chemistry. 12 (6), 789-796

Barrett, ML., Harvey, I., Sundararajan, M., Surendran, R., Hall, JF., Ellis, MJ., Hough, MA., Strange, RW., Hillier, IH. and Hasnain, SS., (2006). Atomic Resolution Crystal Structures, EXAFS, and Quantum Chemical Studies of Rusticyanin and Its Two Mutants Provide Insight into Its Unusual Properties^,. Biochemistry. 45 (9), 2927-2939

Strange, RW., Antonyuk, SV., Hough, MA., Doucette, PA., Valentine, JS. and Hasnain, SS., (2006). Variable Metallation of Human Superoxide Dismutase: Atomic Resolution Crystal Structures of Cu–Zn, Zn–Zn and As-isolated Wild-type Enzymes. Journal of Molecular Biology. 356 (5), 1152-1162

Paraskevopoulos, K., Sundararajan, M., Surendran, R., Hough, MA., Eady, RR., Hillier, IH. and Hasnain, SS., (2006). Active site structures and the redox properties of blue copper proteins: atomic resolution structure of azurin II and electronic structure calculations of azurin, plastocyanin and stellacyanin. Dalton Transactions (25), 3067-3067

Antonyuk, S., Elam, JS., Hough, MA., Strange, RW., Doucette, PA., Rodriguez, JA., Hayward, LJ., Valentine, JS., Hart, PJ. and Hasnain, SS., (2005). Structural consequences of the familial amyotrophic lateral sclerosis SOD1 mutant His46Arg. Protein Science. 14 (5), 1201-1213

Hough, MA., Ellis, MJ., Antonyuk, S., Strange, RW., Sawers, G., Eady, RR. and Samar Hasnain, S., (2005). High Resolution Structural Studies of Mutants Provide Insights into Catalysis and Electron Transfer Processes in Copper Nitrite Reductase. Journal of Molecular Biology. 350 (2), 300-309

Hough, MA., Grossmann, JG., Antonyuk, SV., Strange, RW., Doucette, PA., Rodriguez, JA., Whitson, LJ., Hart, PJ., Hayward, LJ., Valentine, JS. and Hasnain, SS., (2004). Dimer destabilization in superoxide dismutase may result in disease-causing properties: Structures of motor neuron disease mutants. Proceedings of the National Academy of Sciences. 101 (16), 5976-5981

Barrett, ML., Harris, RL., Antonyuk, S., Hough, MA., Ellis, MJ., Sawers, G., Eady, RR. and Hasnain, SS., (2004). Insights into Redox Partner Interactions and Substrate Binding in Nitrite Reductase from Alcaligenes xylosoxidans: Crystal Structures of the Trp138His and His313Gln Mutants^,. Biochemistry. 43 (51), 16311-16319

Strange, RW., Antonyuk, S., Hough, MA., Doucette, PA., Rodriguez, JA., Hart, PJ., Hayward, LJ., Valentine, JS. and Hasnain, SS., (2003). The Structure of Holo and Metal-deficient Wild-type Human Cu, Zn Superoxide Dismutase and its Relevance to Familial Amyotrophic Lateral Sclerosis. Journal of Molecular Biology. 328 (4), 877-891

Hough, MA. and Hasnain, SS., (2003). Structure of Fully Reduced Bovine Copper Zinc Superoxide Dismutase at 1.15 Å. Structure. 11 (8), 937-946

Kanbi, LD., Antonyuk, S., Hough, MA., Hall, JF., Dodd, FE. and Hasnain, SS., (2002). Crystal Structures of the Met148Leu and Ser86Asp Mutants of Rusticyanin from Thiobacillus ferrooxidans: Insights into the Structural Relationship with the Cupredoxins and the Multi Copper Proteins. Journal of Molecular Biology. 320 (2), 263-275

Hough, MA., Hall, JF., Kanbi, LD. and Hasnain, SS., (2001). Structure of the M148Q mutant of rusticyanin at 1.5 Å: a model for the copper site of stellacyanin. Acta Crystallographica Section D Biological Crystallography. 57 (3), 355-360

Hough, MA., Strange, RW. and Hasnain, SS., (2000). Conformational variability of the Cu site in one subunit of bovine CuZn superoxide dismutase: the importance of mobility in the Glu119-Leu142 loop region for catalytic function. Journal of Molecular Biology. 304 (2), 231-241

Ockwell, DM., Hough, MA., Grossmann, JG., Hasnain, SS. and Hao, Q., (2000). Implementation of cluster analysis forab initiophasing using the molecular envelope from solution X-ray scattering. Acta Crystallographica Section D Biological Crystallography. 56 (8), 1002-1006

Hough, MA. and Hasnain, SS., (1999). Crystallographic structures of bovine copper-zinc superoxide dismutase reveal asymmetry in two subunits: functionally important three and five coordinate copper sites captured in the same crystal. Journal of Molecular Biology. 287 (3), 579-592

Hough, M., (2006). Using project and risk management to add capability to your organisation